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BPC-157 with Arginine Salt
SKU: BPC1505M
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Contact Us →BPC-157 is a synthetic 15-amino-acid pentadecapeptide derived from the gastric mucosal protein BPC. In vitro studies document interactions with VEGFR2, EGFR, and FAK phosphorylation cascades, with modulation of pro-angiogenic signalling networks. Preclinical in vivo models have examined its effects on nitric oxide synthase activity, extracellular matrix protein expression, and actin cytoskeletal dynamics in connective tissue contexts.
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3D Molecular Structure of C68H112N20O24
CarbonHydrogenFluorineNitrogenOxygenSulfur
| Chemical Formula | C68H112N20O24 |
|---|---|
| Synonyms | Body Protection Compound-157, Bepecin, PL 14736 |
| Molar Mass | 1,419.5 g/mol |
| CAS Number | 137525-51-0 |
| PubChem CID | 175763564 |
| Total Compound Content | 5 mg per vial |
| Shelf Life | 36 months |
BPC-157 is a synthetic pentadecapeptide (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) identified as a partial sequence of the gastric cytoprotective protein BPC. In cell-based assays, BPC-157 potentiates VEGFR2 phosphorylation and downstream ERK1/2 activation, implicating modulation of pro-angiogenic signalling axes. Additional in vitro data indicate upregulation of focal adhesion kinase (FAK) activity and actin cytoskeletal reorganisation, consistent with observed effects on cell migration in scratch-wound models. In preclinical in vivo studies, administration is associated with eNOS expression upregulation, collagen fibril remodelling, and fibroblast proliferation responses — processes of interest across connective tissue biology, angiogenesis research, and extracellular matrix remodelling models. The peptide exhibits stability across physiological pH and is supplied lyophilised for laboratory reconstitution. Independently third-party HPLC-tested; COA available per batch.
BPC-157 with Arginine Salt 5mg (HPLC)
June 25, 2026 · Janoshik
BPC-157 (GC-MS/LC-MS Contamination Screening)
June 17, 2026 · Janoshik
BPC-157 (Heavy Metal)
June 16, 2026 · Janoshik
Why does BPC-157 demonstrate greater stability than many peptide-based research compounds?
BPC-157 contains multiple proline-rich motifs that are believed to contribute to resistance against enzymatic degradation under a range of experimental conditions. This structural characteristic distinguishes it from many peptide-based research compounds and has contributed to interest in its biochemical stability, peptide persistence, and signaling activity in mechanistic investigations.
What is the relationship between BPC-157 and VEGFR2/FAK signaling pathways?
Experimental investigations have reported enhanced VEGFR2 phosphorylation together with increased focal adhesion kinase (FAK) activity and downstream ERK1/2 signaling. These observations have positioned BPC-157 as a useful research tool for studying angiogenic signaling networks, cellular migration processes, cytoskeletal organization, and extracellular matrix-associated pathway regulation.
How does BPC-157 differ from TB-500 in mechanistic research?
BPC-157 and TB-500 are frequently compared because they influence distinct signaling networks. Research involving BPC-157 has focused primarily on VEGFR2, FAK, ERK1/2, eNOS, and extracellular matrix-associated pathways, whereas TB-500 investigations emphasize actin dynamics, cytoskeletal organization, cell migration, and tissue remodeling mechanisms. Their differing mechanistic profiles make them valuable tools for comparative studies of peptide-mediated signaling and cellular regulatory processes.
